[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Thymus; DOI=10.1093/nar/14.14.5777; PubMed=3755527 [NCBI, ExPASy, EBI, Israel, Japan] Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.; "Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells."; Nucleic Acids Res. 14:5777-5792(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Thymus; NIH - Mammalian Gene Collection (MGC) project; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-2. DOI=10.1016/S0006-291X(87)80493-X; PubMed=3579900 [NCBI, ExPASy, EBI, Israel, Japan] Koiwai O., Kaneda T., Morishita R.; "Analysis of human terminal deoxynucleotidyl transferase cDNA expressible in mammalian cells."; Biochem. Biophys. Res. Commun. 144:185-190(1987).
[4]	PROTEIN SEQUENCE OF 132-168; 169-176; 183-188; 191-219; 223-334; 336-415 AND 421-509. DOI=10.1021/bi00428a045; PubMed=2713339 [NCBI, ExPASy, EBI, Israel, Japan] Evans R.K., Beach C.M., Coleman M.S.; "Photoaffinity labeling of terminal deoxynucleotidyl transferase. 2. Identification of peptides in the nucleotide binding domain."; Biochemistry 28:713-720(1989).
[5]	PARTIAL PROTEIN SEQUENCE OF 210-238. PubMed=3346221 [NCBI, ExPASy, EBI, Israel, Japan] Pandey V.N., Modak M.J.; "Biochemistry of terminal deoxynucleotidyltransferase. Affinity labeling and identification of the deoxynucleoside triphosphate binding domain of terminal deoxynucleotidyltransferase."; J. Biol. Chem. 263:3744-3751(1988).
[6]	PROTEIN SEQUENCE OF 210-221 AND 224-238, AND ATP- AND DTTP-BINDING SITES CYS-216 AND CYS-224. PubMed=2910867 [NCBI, ExPASy, EBI, Israel, Japan] Pandey V.N., Modak M.J.; "Biochemistry of terminal deoxynucleotidyltransferase. Identification and unity of ribo- and deoxyribonucleoside triphosphate binding site in terminal deoxynucleotidyltransferase."; J. Biol. Chem. 264:867-871(1989).
[7]	PROTEIN SEQUENCE OF 306-326; 337-357 AND 483-506. PubMed=6087320 [NCBI, ExPASy, EBI, Israel, Japan] Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.; "Molecular cloning of human terminal deoxynucleotidyltransferase."; Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984).

Comments

FUNCTION: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
COFACTOR: Magnesium.
SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA (By similarity).
SUBCELLULAR LOCATION: Nucleus.
SIMILARITY: Belongs to the DNA polymerase type-X family.
SIMILARITY: Contains 1 BRCT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X04122; CAA27734.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114820; AAI14821.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26146; AAA87354.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A23595; A23595.

NP_803461.1; -.

3D structure databases

HSSP

P09838; 1JMS. [HSSP ENTRY / PDB]

SMR

P06526; 21-125, 148-509.

ModBase

P06526.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006304;	Biological process: DNA modification (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001357; BRCT.
IPR002054; DNA-dir_DNA_pol_X.
IPR010996; DNA-dir_DNA_pol_X_beta-like_N.
IPR001726; DNA_nucleotidylexotransferase.
IPR002934; Nucleotidyltransferase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.150.110; DNA_pol_b_N-like; 1.

PANTHER

PTHR11276:SF6; DNA_polXtrans; 1.

Pfam

PF00533; BRCT; 1.
PF01909; NTP_transf_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000817; DNA_NT; 1.

PRINTS

PR00869; DNAPOLX.
PR00871; DNAPOLXTDT.

SMART

SM00292; BRCT; 1.
SM00483; POLXc; 1.
SMART graphical view of domain structure.

PROSITE

PS50172; BRCT; 1.
PS00522; DNA_POLYMERASE_X; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000020427; Bos taurus. [Contig view]

GeneID

281120; -.

KEGG

bta:281120; -.

Phylogenomic databases

HOVERGEN

P06526; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Terminal addition; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 509`	`509`	`DNA nucleotidylexotransferase.`	`PRO_0000218790`
`DOMAIN`	`27 124`	`98`	`BRCT.`
`REGION`	`151 509`	`359`	`Mediates interaction with DNTTIP2 (By similarity).`
`REGION`	`336 345`	`10`	`Involved in ssDNA binding (By similarity).`
`METAL`	`253 253`		`Sodium; via carbonyl oxygen (By similarity).`
`METAL`	`255 255`		`Sodium; via carbonyl oxygen (By similarity).`
`METAL`	`343 343`		`Magnesium (By similarity).`
`METAL`	`345 345`		`Magnesium (By similarity).`
`METAL`	`433 433`		`Magnesium (By similarity).`

Sequence information

Length: 509 AA [This is the length of the unprocessed precursor]

Molecular weight: 58296 Da [This is the MW of the unprocessed precursor]

CRC64: EE5262617BA5D207 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDPLCTASSG PRKKRPRQVG ASMASPPHDI KFQNLVLFIL EKKMGTTRRN FLMELARRKG 

        70         80         90        100        110        120 
FRVENELSDS VTHIVAENNS GSEVLEWLQV QNIRASSQLE LLDVSWLIES MGAGKPVEIT 

       130        140        150        160        170        180 
GKHQLVVRTD YSATPNPGFQ KTPPLAVKKI SQYACQRKTT LNNYNHIFTD AFEILAENSE 

       190        200        210        220        230        240 
FKENEVSYVT FMRAASVLKS LPFTIISMKD TEGIPCLGDK VKCIIEEIIE DGESSEVKAV 

       250        260        270        280        290        300 
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRSLSKIMSD KTLKFTKMQK AGFLYYEDLV 

       310        320        330        340        350        360 
SCVTRAEAEA VGVLVKEAVW AFLPDAFVTM TGGFRRGKKI GHDVDFLITS PGSAEDEEQL 

       370        380        390        400        410        420 
LPKVINLWEK KGLLLYYDLV ESTFEKFKLP SRQVDTLDHF QKCFLILKLH HQRVDSSKSN 

       430        440        450        460        470        480 
QQEGKTWKAI RVDLVMCPYE NRAFALLGWT GSRQFERDIR RYATHERKMM LDNHALYDKT 

       490        500 
KRVFLKAESE EEIFAHLGLD YIEPWERNA

P06526 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools